Search results for: Caspase-1 Inhibitor Z-YVAD-FMK
#29039567 2017/10/17 Save this To Up
Leptin promotes IL‑18 secretion by activating the NLRP3 inflammasome in RAW 264.7 cells.Leptin is a cytokine‑like hormone secreted by adipocytes, which serves to control energy expenditure and metabolism. In addition, leptin may modulate the innate and adaptive immune responses. The innate immune cell sensor nucleotide‑binding oligomerization domain‑like receptor family pyrin domain‑containing 3 (NLRP3) inflammasome is mainly expressed in myeloid immune cells, including macrophages. The NLRP3 inflammasome serves a pivotal role in the development and maintenance of autoimmunity and inflammation. The expression levels of caspase‑1, apoptosis‑associated speck‑like protein containing a CARD, interleukin (IL)‑18, IL‑1β and leptin are significantly reduced in the white adipose tissue of nonsteroidal anti‑inflammatory drug‑activated gene‑1 transgenic mice. However, the association between leptin and the NLRP3 inflammasome has not yet to be determined. The aim of the present study, was to explore the role of leptin on NLRP3 inflammasome. In order to do this, IL‑1β and IL‑18 expression levels were investigated in RAW 264.7 cells after incubation with leptin of increasing doses by Elisa or reverse transcription‑quantitative polymerase chain reaction, and to assess whether IL‑1β and IL‑18 were affected after caspase‑1 activity being inhibited by an inhibitor or by silencing NLRP3 expression. The results of the present study demonstrated that leptin enhanced the mRNA and protein expression levels of IL‑18 in RAW 264.7 cells via activation of the NLRP3 inflammasome. This is achieved partly by enhancing the production of reactive oxygen species and K+ efflux. Therefore, leptin may be considered a novel activator and modulator of the NLRP3 inflammasome.
2625 related Products with: Leptin promotes IL‑18 secretion by activating the NLRP3 inflammasome in RAW 264.7 cells.Recombinant Porcine Inter Recombinant Porcine Inter Recombinant Porcine Inter GLP 1 ELISA Kit, Rat Gluc Leptin ELISA Kit, Rat Lep BYL-719 Mechanisms: PI3K- Interleukins Recombinant Interleukins Recombinant anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl CELLKINES Natural Human I
#28854426 2017/08/30 Save this To Up
Autophagy Inhibition Contributes to ROS-Producing NLRP3-Dependent Inflammasome Activation and Cytokine Secretion in High Glucose-Induced Macrophages.Type 2 diabetes is a persistent inflammatory response that impairs the healing process. We hypothesized that stimulation with high glucose following a pro-inflammatory signal would lead to autophagy inhibition, reactive oxygen species (ROS) production and eventually to the activation of the Nod-like receptor protein (NLRP) -3.
2646 related Products with: Autophagy Inhibition Contributes to ROS-Producing NLRP3-Dependent Inflammasome Activation and Cytokine Secretion in High Glucose-Induced Macrophages.Cell Meter™ Fluorimetri Cell Meter™ Fluorimetri GLP 1 ELISA Kit, Rat Gluc Cytokine antibody array i Insulin Glucose Phospho-S Cytokine (Human) Antibody Cytokine (Human) Antibody Cytokine (Human) Antibody Cytokine (Human) Antibody Cytokine (Human) Antibody Cytokine (Human) Antibody Cytokine (Human) Antibody
#28245402 2017/02/28 Save this To Up
[Caspase1 Inhibitor Ac-YVAD-CMK Prevents and Treats the Acute Graft Versus Host Disease in Mice].To explore the effect of Caspase 1 inhibitor Ac-YVAD-CMK on acute graft-versus-host disease (aGVHD) after allogeneic hematopoietic stem cell transplantation(allo-HSCT) and its mechanism.
1743 related Products with: [Caspase1 Inhibitor Ac-YVAD-CMK Prevents and Treats the Acute Graft Versus Host Disease in Mice].Caspase-1 Inhibitor Z-YVA Caspase-1 Inhibitor Z-YVA Caspase 1 Inhibitor Z YVA Caspase 1 Inhibitor Z YVA Caspase-1 Inhibitor Z-YVA Caspase-1 Inhibitor Z-YVA Caspase 1 Inhibitor Z YVA Caspase 1 Inhibitor Z YVA Granzyme B Inhibitor (Z A Hamster AntiSerine Protea Hamster AntiSerine Protea anti-Diazepam Binding Inh
#27320880 2016/06/20 Save this To Up
[NLRP3 inflammasome mediates angiotension II-induced expression of inflammatory factor interleukin-1β in human umbilical vein endothelial cells].To investigate the effect of angiotension II (AngII) on the activation of NLRP3 inflammasome and the expression of interleukin-1β (IL-1β) in human umbilical vein endothelial cells (HUVECs).
1286 related Products with: [NLRP3 inflammasome mediates angiotension II-induced expression of inflammatory factor interleukin-1β in human umbilical vein endothelial cells].Human Umbilical Vein Endo GFP Expressing Human Umbi Mitochondria GFP Tag Huma Plasma Membrane GFP Tag H RFP Expressing Human Umbi Human Insulin-like Growth Macrophage Colony Stimula Macrophage Colony Stimula TGF beta induced factor 2 Human Small Intestine Mic Human Large Intestine Mic Human Internal Mammary Ar
#26935015 2016/04/07 Save this To Up
Release mechanism of high mobility group nucleosome binding domain 1 from lipopolysaccharide-stimulated macrophages.Alarmins are identified as endogenous mediators that have potent immune-activating abilities. High mobility group nucleosome binding domain 1 (HMGN1), a highly conserved, non-histone chromosomal protein, which binds to the inner side of the nucleosomal DNA, regulates chromatin dynamics and transcription in cells. Furthermore, HMGN1 acts as a cytokine in the extracellular milieu by inducing the recruitment and maturation of antigen-presenting cells (dendritic cells) to enhance Th1-type antigen-specific immune responses. Thus, HMGN1 is expected to act as an alarmin, when released into the extracellular milieu. The present study investigated the release mechanism of HMGN1 from macrophages using mouse macrophage‑like RAW264.7 cells. The results indicated that HMGN1 was released from lipopolysaccharide (LPS)‑stimulated RAW264.7 cells, accompanied by cell death as assessed by the release of lactate dehydrogenase (LDH). Subsequently, the patterns of cell death involved in HMGN1 release from LPS‑stimulated RAW264.7 cells were determined using a caspase‑1 inhibitor, YVAD, and a necroptosis inhibitor, Nec‑1. YVAD and Nec‑1 did not alter LPS‑induced HMGN1 and LDH release, suggesting that pyroptosis (caspase‑1‑activated cell death) and necroptosis are not involved in the release of HMGN1 from LPS‑stimulated RAW264.7 cells. In addition, flow cytometric analysis indicated that LPS stimulation did not induce apoptosis but substantially augmented necrosis, as evidenced by staining with annexin V/propidium iodide. Together these findings suggest that HMGN1 is extracellularly released from LPS‑stimulated RAW264.7 macrophage‑like cells, accompanied by unprogrammed necrotic cell death but not pyroptosis, necroptosis or apoptosis.
1444 related Products with: Release mechanism of high mobility group nucleosome binding domain 1 from lipopolysaccharide-stimulated macrophages.HMG2 (High mobility group SH3 domain-binding protei Human High Mobility Group Monoclonal Anti-Cellulose DAB Substrate (High Cont DAB Chromogen Substrate ELISA Binding Buffer ELISA Binding Buffer Naphthol Phosphate Buffe Naphthol Phosphate Buffe TMB Soluble Reagent (Hig TMB Soluble Reagent (Hig
#12527914 2003/01/15 Save this To Up
Thiol alkylation inhibits the mitogenic effects of platelet-derived growth factor and renders it proapoptotic via activation of STATs and p53 and induction of expression of caspase1 and p21(waf1/cip1).Thiols provide the major intracellular redox milieu and can undergo reversible oxidation and reduction. To understand the role of thiols in redox signaling events, we have studied the effect of N-ethylmaleimide, a specific thiol alkylating agent, on platelet-derived growth factor-BB (PDGF-BB)-induced mitogenesis in vascular smooth muscle cells (VSMC). Thiol alkylation inhibited PDGF-BB-induced expression of the Fos and Jun family proteins and AP-1 activity in VSMC. Thiol alkylation also inhibited PDGF-BB-induced expression of cyclin A and growth in these cells. In contrast, thiol alkylation enhanced and sustained the effect of PDGF-BB on the activation of the Jak STAT pathway, and this event was correlated with inhibition of protein tyrosine phosphatase lB activity. Thiol alkylation via inducing the expression of p21(waf1/cip1) in a STAT1- and p53-dependent manner antagonized the downregulation of this cell cycle inhibitory molecule by PDGF-BB. The inhibition of AP-1 and activation of STATs, particularly STAT1, by thiol alkylation correlated with increased production of active caspase 1 and apoptosis in VSMC. Together, these findings suggest a role for thiols in mediating mitogenic and/or apoptotic signaling events in VSMC. These results also show that a sustained change in the intracellular thiol redox state can convert a mitogen into a death promoter.
2978 related Products with: Thiol alkylation inhibits the mitogenic effects of platelet-derived growth factor and renders it proapoptotic via activation of STATs and p53 and induction of expression of caspase1 and p21(waf1/cip1).CELLKINES PLATELET DERIVE PLATELET DERIVED GROWTH F CELLKINES PLATELET DERIVE PLATELET DERIVED GROWTH F Human Platelet Derived Gr Human Platelet Derived Gr Human Platelet Derived Gr Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Mouse Platelet Derived Gr
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